ID CC50A_HUMAN Reviewed; 361 AA. AC Q9NV96; A8K9V8; E1P539; Q658Z3; Q96H09; Q9NSL9; DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 158. DE RecName: Full=Cell cycle control protein 50A {ECO:0000305}; DE AltName: Full=P4-ATPase flippase complex beta subunit TMEM30A; DE AltName: Full=Transmembrane protein 30A; GN Name=TMEM30A {ECO:0000312|HGNC:HGNC:16667}; Synonyms=C6orf67, CDC50A; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Amygdala, Lymph node, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP IDENTIFICATION. RX PubMed=15375526; RA Katoh Y., Katoh M.; RT "Identification and characterization of CDC50A, CDC50B and CDC50C genes in RT silico."; RL Oncol. Rep. 12:939-943(2004). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-294. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-190. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [10] RP FUNCTION. RX PubMed=20510206; DOI=10.1016/j.bcp.2010.05.017; RA Munoz-Martinez F., Torres C., Castanys S., Gamarro F.; RT "CDC50A plays a key role in the uptake of the anticancer drug perifosine in RT human carcinoma cells."; RL Biochem. Pharmacol. 80:793-800(2010). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP8A1; ATP8A2; RP ATP8B1; ATP8B2 AND ATP8B4. RX PubMed=20947505; DOI=10.1074/jbc.m110.139006; RA van der Velden L.M., Wichers C.G., van Breevoort A.E., Coleman J.A., RA Molday R.S., Berger R., Klomp L.W., van de Graaf S.F.; RT "Heteromeric interactions required for abundance and subcellular RT localization of human CDC50 proteins and class 1 P4-ATPases."; RL J. Biol. Chem. 285:40088-40096(2010). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP8A1; ATP8B1; ATP8B2 RP AND ATP8B4. RX PubMed=20961850; DOI=10.1074/jbc.m110.139543; RA Bryde S., Hennrich H., Verhulst P.M., Devaux P.F., Lenoir G., RA Holthuis J.C.; RT "CDC50 proteins are critical components of the human class-1 P4-ATPase RT transport machinery."; RL J. Biol. Chem. 285:40562-40572(2010). RN [13] RP INTERACTION WITH ATP8A2. RX PubMed=21454556; DOI=10.1074/jbc.m111.229419; RA Coleman J.A., Molday R.S.; RT "Critical role of the beta-subunit CDC50A in the stable expression, RT assembly, subcellular localization, and lipid transport activity of the P4- RT ATPase ATP8A2."; RL J. Biol. Chem. 286:17205-17216(2011). RN [14] RP INTERACTION WITH ATP11A; ATP11B AND ATP11C, AND SUBCELLULAR LOCATION. RX PubMed=21914794; DOI=10.1074/jbc.m111.281006; RA Takatsu H., Baba K., Shima T., Umino H., Kato U., Umeda M., Nakayama K., RA Shin H.W.; RT "ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes RT to the trans-Golgi network in a CDC50 protein-independent manner."; RL J. Biol. Chem. 286:38159-38167(2011). RN [15] RP FUNCTION. RX PubMed=21289302; DOI=10.4049/jimmunol.1002710; RA Chen R., Brady E., McIntyre T.M.; RT "Human TMEM30a promotes uptake of antitumor and bioactive choline RT phospholipids into mammalian cells."; RL J. Immunol. 186:3215-3225(2011). RN [16] RP FUNCTION, AND INTERACTION WITH ATP8B1; ATP10A; ATP10B; ATP10D AND ATP11A. RX PubMed=25947375; DOI=10.1074/jbc.m115.655191; RA Naito T., Takatsu H., Miyano R., Takada N., Nakayama K., Shin H.W.; RT "Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and Is RT Involved in Plasma Membrane Dynamics."; RL J. Biol. Chem. 290:15004-15017(2015). RN [17] RP FUNCTION, AND INTERACTION WITH ATP11A. RX PubMed=29799007; DOI=10.1038/s41467-018-04436-w; RA Tsuchiya M., Hara Y., Okuda M., Itoh K., Nishioka R., Shiomi A., Nagao K., RA Mori M., Mori Y., Ikenouchi J., Suzuki R., Tanaka M., Ohwada T., Aoki J., RA Kanagawa M., Toda T., Nagata Y., Matsuda R., Takayama Y., Tominaga M., RA Umeda M.; RT "Cell surface flip-flop of phosphatidylserine is critical for PIEZO1- RT mediated myotube formation."; RL Nat. Commun. 9:2049-2049(2018). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.90 ANGSTROMS) IN COMPLEX WITH ATP11C, FUNCTION, RP AND MUTAGENESIS OF ARG-132; ARG-133 AND LYS-136. RX PubMed=32493773; DOI=10.1074/jbc.ra120.014144; RA Nakanishi H., Irie K., Segawa K., Hasegawa K., Fujiyoshi Y., Nagata S., RA Abe K.; RT "Crystal structure of a human plasma membrane phospholipid flippase."; RL J. Biol. Chem. 295:10180-10194(2020). RN [19] RP STRUCTURE BY ELECTRON MICROSCOPY (2.83 ANGSTROMS)IN COMPLEX WITH ATP8A1, RP DISULFIDE BONDS, GLYCOSYLATION AT ASN-107; ASN-180 AND ASN-294, AND RP INTERACTION WITH ATP8A1. RX PubMed=31416931; DOI=10.1126/science.aay3353; RA Hiraizumi M., Yamashita K., Nishizawa T., Nureki O.; RT "Cryo-EM structures capture the transport cycle of the P4-ATPase RT flippase."; RL Science 365:1149-1155(2019). CC -!- FUNCTION: Accessory component of a P4-ATPase flippase complex which CC catalyzes the hydrolysis of ATP coupled to the transport of CC aminophospholipids from the outer to the inner leaflet of various CC membranes and ensures the maintenance of asymmetric distribution of CC phospholipids. Phospholipid translocation seems also to be implicated CC in vesicle formation and in uptake of lipid signaling molecules. The CC beta subunit may assist in binding of the phospholipid substrate. CC Required for the proper folding, assembly and ER to Golgi exit of the CC ATP8A2:TMEM30A flippase complex. ATP8A2:TMEM30A may be involved in CC regulation of neurite outgrowth, and, reconstituted to liposomes, CC predomiminantly transports phosphatidylserine (PS) and to a lesser CC extent phosphatidylethanolamine (PE). The ATP8A1:TMEM30A flippase CC complex seems to play a role in regulation of cell migration probably CC involving flippase-mediated translocation of phosphatidylethanolamine CC (PE) at the plasma membrane. Required for the formation of the ATP8A2, CC ATP8B1 and ATP8B2 P-type ATPAse intermediate phosphoenzymes. Involved CC in uptake of platelet-activating factor (PAF), synthetic drug CC alkylphospholipid edelfosine, and, probably in association with ATP8B1, CC of perifosine. Also mediates the export of alpha subunits ATP8A1, CC ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B and CC ATP11C from the ER to other membrane localizations. CC {ECO:0000269|PubMed:20510206, ECO:0000269|PubMed:20947505, CC ECO:0000269|PubMed:20961850, ECO:0000269|PubMed:21289302, CC ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29799007, CC ECO:0000269|PubMed:32493773}. CC -!- SUBUNIT: Component of various P4-ATPase flippase complexes which CC consists of a catalytic alpha subunit and an accessory beta subunit CC (PubMed:31416931). Interacts with ATP8A1 to form a flippase complex; CC this complex forms an intermediate phosphoenzyme (PubMed:31416931). The CC ATP8A2:TMEM30A flippase complex has been purified, and ATP8B1:TMEM30A CC and ATP8B2:TMEM30A flippase complexes have been shown to form CC intermediate phosphoenzymes in vitro. Interacts with alpha subunits CC ATP8A1, ATP8B1, ATP8B2, ATP8B4, ATP10A, ATP10B, ATP10D, ATP11A, ATP11B CC and ATP11C. {ECO:0000269|PubMed:20947505, ECO:0000269|PubMed:20961850, CC ECO:0000269|PubMed:21454556, ECO:0000269|PubMed:21914794, CC ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:29799007, CC ECO:0000269|PubMed:31416931, ECO:0000269|PubMed:32493773}. CC -!- INTERACTION: CC Q9NV96; O60312: ATP10A; NbExp=3; IntAct=EBI-2836942, EBI-26444318; CC Q9NV96; P98196: ATP11A; NbExp=4; IntAct=EBI-2836942, EBI-21519640; CC Q9NV96; Q9Y2G3: ATP11B; NbExp=2; IntAct=EBI-2836942, EBI-20857228; CC Q9NV96; Q8NB49: ATP11C; NbExp=2; IntAct=EBI-2836942, EBI-11279131; CC Q9NV96; Q9Y2Q0: ATP8A1; NbExp=5; IntAct=EBI-2836942, EBI-9539324; CC Q9NV96; Q9Y2Q0-2: ATP8A1; NbExp=2; IntAct=EBI-2836942, EBI-21654619; CC Q9NV96; O43520: ATP8B1; NbExp=9; IntAct=EBI-2836942, EBI-9524729; CC Q9NV96; P98198: ATP8B2; NbExp=4; IntAct=EBI-2836942, EBI-9539266; CC Q9NV96; Q8TF62: ATP8B4; NbExp=4; IntAct=EBI-2836942, EBI-9527207; CC Q9NV96-1; O94823-1: ATP10B; NbExp=2; IntAct=EBI-26444832, EBI-26444823; CC Q9NV96-2; P54253: ATXN1; NbExp=6; IntAct=EBI-12921610, EBI-930964; CC Q9NV96-2; P42858: HTT; NbExp=3; IntAct=EBI-12921610, EBI-466029; CC Q9NV96-2; P21145: MAL; NbExp=3; IntAct=EBI-12921610, EBI-3932027; CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane CC protein {ECO:0000250}. Cell membrane. Golgi apparatus. Cytoplasmic CC vesicle, secretory vesicle membrane {ECO:0000250}. Apical cell membrane CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9NV96-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NV96-2; Sequence=VSP_019568; CC Name=3; CC IsoId=Q9NV96-3; Sequence=VSP_019567; CC -!- DOMAIN: The N-terminal domain seems to play a role in the reaction CC cycle of the catalytic subunit such as ATP8A2. {ECO:0000250}. CC -!- PTM: N-glycosylated. Contains high mannose-type oligosaccharides (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK001718; BAA91859.1; -; mRNA. DR EMBL; AK292823; BAF85512.1; -; mRNA. DR EMBL; AL832815; CAH56262.1; -; mRNA. DR EMBL; AL832490; CAH56205.1; -; mRNA. DR EMBL; AL162046; CAB82389.1; -; mRNA. DR EMBL; AL080250; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471051; EAW48743.1; -; Genomic_DNA. DR EMBL; CH471051; EAW48744.1; -; Genomic_DNA. DR EMBL; CH471051; EAW48745.1; -; Genomic_DNA. DR EMBL; BC009006; AAH09006.1; -; mRNA. DR CCDS; CCDS47453.1; -. [Q9NV96-2] DR CCDS; CCDS4983.1; -. [Q9NV96-1] DR PIR; T47140; T47140. DR RefSeq; NP_001137430.1; NM_001143958.1. [Q9NV96-2] DR RefSeq; NP_060717.1; NM_018247.3. [Q9NV96-1] DR PDB; 6K7G; EM; 3.30 A; C=1-361. DR PDB; 6K7H; EM; 3.22 A; C=1-361. DR PDB; 6K7I; EM; 3.22 A; C=1-361. DR PDB; 6K7J; EM; 3.08 A; C=1-361. DR PDB; 6K7K; EM; 3.04 A; C=1-361. DR PDB; 6K7L; EM; 2.83 A; C=1-361. DR PDB; 6K7M; EM; 2.95 A; C=1-361. DR PDB; 6K7N; EM; 2.84 A; C=1-361. DR PDB; 6LKN; X-ray; 3.90 A; C/F/J/N=1-361. DR PDB; 7BSP; EM; 4.00 A; C=1-361. DR PDB; 7BSQ; EM; 3.20 A; C=1-361. DR PDB; 7BSS; EM; 3.30 A; C=1-361. DR PDB; 7BSU; EM; 3.20 A; C=1-361. DR PDB; 7BSV; EM; 3.00 A; C=1-361. DR PDB; 7BSW; EM; 3.90 A; C=1-361. DR PDB; 7PY4; EM; 3.10 A; B=25-351. DR PDB; 7VGI; EM; 3.36 A; A=1-361. DR PDB; 7VGJ; EM; 3.98 A; B=1-361. DR PDB; 7VSG; EM; 3.90 A; B=1-361. DR PDB; 7VSH; EM; 3.40 A; C=1-361. DR PDB; 8OX4; EM; 3.40 A; B=1-361. DR PDB; 8OX5; EM; 2.90 A; B=1-361. DR PDB; 8OX6; EM; 2.39 A; B=1-361. DR PDB; 8OX7; EM; 2.56 A; B=1-361. DR PDB; 8OX8; EM; 2.98 A; B=1-361. DR PDB; 8OX9; EM; 2.72 A; B=1-361. DR PDB; 8OXA; EM; 2.76 A; B=1-361. DR PDB; 8OXB; EM; 2.99 A; B=1-361. DR PDB; 8OXC; EM; 2.58 A; B=1-361. DR PDBsum; 6K7G; -. DR PDBsum; 6K7H; -. DR PDBsum; 6K7I; -. DR PDBsum; 6K7J; -. DR PDBsum; 6K7K; -. DR PDBsum; 6K7L; -. DR PDBsum; 6K7M; -. DR PDBsum; 6K7N; -. DR PDBsum; 6LKN; -. DR PDBsum; 7BSP; -. DR PDBsum; 7BSQ; -. DR PDBsum; 7BSS; -. DR PDBsum; 7BSU; -. DR PDBsum; 7BSV; -. DR PDBsum; 7BSW; -. DR PDBsum; 7PY4; -. DR PDBsum; 7VGI; -. DR PDBsum; 7VGJ; -. DR PDBsum; 7VSG; -. DR PDBsum; 7VSH; -. DR PDBsum; 8OX4; -. DR PDBsum; 8OX5; -. DR PDBsum; 8OX6; -. DR PDBsum; 8OX7; -. DR PDBsum; 8OX8; -. DR PDBsum; 8OX9; -. DR PDBsum; 8OXA; -. DR PDBsum; 8OXB; -. DR PDBsum; 8OXC; -. DR AlphaFoldDB; Q9NV96; -. DR EMDB; EMD-13711; -. DR EMDB; EMD-17256; -. DR EMDB; EMD-17257; -. DR EMDB; EMD-17258; -. DR EMDB; EMD-17259; -. DR EMDB; EMD-17260; -. DR EMDB; EMD-17261; -. DR EMDB; EMD-17262; -. DR EMDB; EMD-17263; -. DR EMDB; EMD-17264; -. DR EMDB; EMD-30163; -. DR EMDB; EMD-30164; -. DR EMDB; EMD-30165; -. DR EMDB; EMD-30167; -. DR EMDB; EMD-30168; -. DR EMDB; EMD-30169; -. DR EMDB; EMD-31970; -. DR EMDB; EMD-31971; -. DR EMDB; EMD-32110; -. DR EMDB; EMD-32111; -. DR EMDB; EMD-9931; -. DR EMDB; EMD-9932; -. DR EMDB; EMD-9933; -. DR EMDB; EMD-9934; -. DR EMDB; EMD-9935; -. DR EMDB; EMD-9936; -. DR EMDB; EMD-9937; -. DR EMDB; EMD-9938; -. DR EMDB; EMD-9939; -. DR EMDB; EMD-9940; -. DR EMDB; EMD-9941; -. DR EMDB; EMD-9942; -. DR SMR; Q9NV96; -. DR BioGRID; 120872; 165. DR ComplexPortal; CPX-6282; ATP8B1-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6285; ATP8A1-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6301; ATP8A2-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6302; ATP8B2-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6304; ATP8B3-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6305; ATP8B4-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6307; ATP10A-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6308; ATP10B-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6309; ATP10D-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6310; ATP11A-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6311; ATP11B-CDC50A P4-ATPase complex. DR ComplexPortal; CPX-6312; ATP11C-CDC50A P4-ATPase complex. DR IntAct; Q9NV96; 63. DR MINT; Q9NV96; -. DR STRING; 9606.ENSP00000230461; -. DR TCDB; 1.A.17.1.30; the calcium-dependent chloride channel (ca-clc) family. DR TCDB; 8.A.27.1.5; the cdc50 p-type atpase lipid flippase subunit (cdc50) family. DR GlyCosmos; Q9NV96; 4 sites, No reported glycans. DR GlyGen; Q9NV96; 6 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q9NV96; -. DR PhosphoSitePlus; Q9NV96; -. DR SwissPalm; Q9NV96; -. DR BioMuta; TMEM30A; -. DR DMDM; 74752991; -. DR EPD; Q9NV96; -. DR jPOST; Q9NV96; -. DR MassIVE; Q9NV96; -. DR MaxQB; Q9NV96; -. DR PaxDb; 9606-ENSP00000230461; -. DR PeptideAtlas; Q9NV96; -. DR ProteomicsDB; 82763; -. [Q9NV96-1] DR ProteomicsDB; 82764; -. [Q9NV96-2] DR ProteomicsDB; 82765; -. [Q9NV96-3] DR Pumba; Q9NV96; -. DR Antibodypedia; 31507; 79 antibodies from 24 providers. DR DNASU; 55754; -. DR Ensembl; ENST00000230461.11; ENSP00000230461.6; ENSG00000112697.17. [Q9NV96-1] DR Ensembl; ENST00000370050.9; ENSP00000359067.5; ENSG00000112697.17. [Q9NV96-3] DR Ensembl; ENST00000475111.6; ENSP00000431007.1; ENSG00000112697.17. [Q9NV96-2] DR Ensembl; ENST00000674151.1; ENSP00000500998.1; ENSG00000112697.17. [Q9NV96-3] DR GeneID; 55754; -. DR KEGG; hsa:55754; -. DR MANE-Select; ENST00000230461.11; ENSP00000230461.6; NM_018247.4; NP_060717.1. DR UCSC; uc003phw.3; human. [Q9NV96-1] DR AGR; HGNC:16667; -. DR CTD; 55754; -. DR DisGeNET; 55754; -. DR GeneCards; TMEM30A; -. DR HGNC; HGNC:16667; TMEM30A. DR HPA; ENSG00000112697; Low tissue specificity. DR MIM; 611028; gene. DR neXtProt; NX_Q9NV96; -. DR OpenTargets; ENSG00000112697; -. DR PharmGKB; PA134936902; -. DR VEuPathDB; HostDB:ENSG00000112697; -. DR eggNOG; KOG2952; Eukaryota. DR GeneTree; ENSGT00390000004660; -. DR HOGENOM; CLU_025025_1_0_1; -. DR InParanoid; Q9NV96; -. DR OMA; IPWSMFN; -. DR OrthoDB; 196427at2759; -. DR PhylomeDB; Q9NV96; -. DR TreeFam; TF300873; -. DR PathwayCommons; Q9NV96; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR SignaLink; Q9NV96; -. DR BioGRID-ORCS; 55754; 68 hits in 1171 CRISPR screens. DR ChiTaRS; TMEM30A; human. DR GenomeRNAi; 55754; -. DR Pharos; Q9NV96; Tbio. DR PRO; PR:Q9NV96; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q9NV96; Protein. DR Bgee; ENSG00000112697; Expressed in tendon of biceps brachii and 211 other cell types or tissues. DR ExpressionAtlas; Q9NV96; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0031901; C:early endosome membrane; IDA:ComplexPortal. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central. DR GO; GO:0031902; C:late endosome membrane; IDA:ComplexPortal. DR GO; GO:0016020; C:membrane; IDA:ComplexPortal. DR GO; GO:1990531; C:phospholipid-translocating ATPase complex; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL. DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome. DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015247; F:aminophospholipid flippase activity; IDA:BHF-UCL. DR GO; GO:0005198; F:structural molecule activity; IDA:FlyBase. DR GO; GO:0015917; P:aminophospholipid transport; IDA:BHF-UCL. DR GO; GO:0045332; P:phospholipid translocation; IDA:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0061092; P:positive regulation of phospholipid translocation; IDA:UniProtKB. DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0036010; P:protein localization to endosome; IMP:UniProtKB. DR GO; GO:0006855; P:xenobiotic transmembrane transport; IDA:UniProtKB. DR InterPro; IPR005045; CDC50/LEM3_fam. DR PANTHER; PTHR10926; CELL CYCLE CONTROL PROTEIN 50; 1. DR PANTHER; PTHR10926:SF17; CELL CYCLE CONTROL PROTEIN 50A; 1. DR Pfam; PF03381; CDC50; 1. DR PIRSF; PIRSF015840; DUF284_TM_euk; 1. DR Genevisible; Q9NV96; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Golgi apparatus; KW Lipid transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330" FT CHAIN 2..361 FT /note="Cell cycle control protein 50A" FT /id="PRO_0000244469" FT TOPO_DOM 2..49 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 50..70 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 71..325 FT /note="Exoplasmic loop" FT /evidence="ECO:0000255" FT TRANSMEM 326..346 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 347..361 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 1..29 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330" FT CARBOHYD 107 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:31416931, FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, FT ECO:0007744|PDB:6K7M" FT CARBOHYD 180 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255, ECO:0000269|PubMed:31416931, FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, FT ECO:0007744|PDB:6K7M" FT CARBOHYD 190 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19349973" FT CARBOHYD 294 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:31416931, ECO:0007744|PDB:6K7G, FT ECO:0007744|PDB:6K7H, ECO:0007744|PDB:6K7I, FT ECO:0007744|PDB:6K7J, ECO:0007744|PDB:6K7K, FT ECO:0007744|PDB:6K7L, ECO:0007744|PDB:6K7M" FT DISULFID 91..104 FT /evidence="ECO:0000269|PubMed:31416931, FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, FT ECO:0007744|PDB:6K7M, ECO:0007744|PDB:6K7N" FT DISULFID 94..102 FT /evidence="ECO:0000269|PubMed:31416931, FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, FT ECO:0007744|PDB:6K7M, ECO:0007744|PDB:6K7N" FT DISULFID 157..171 FT /evidence="ECO:0000269|PubMed:31416931, FT ECO:0007744|PDB:6K7G, ECO:0007744|PDB:6K7H, FT ECO:0007744|PDB:6K7I, ECO:0007744|PDB:6K7J, FT ECO:0007744|PDB:6K7K, ECO:0007744|PDB:6K7L, FT ECO:0007744|PDB:6K7M" FT VAR_SEQ 1..119 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_019567" FT VAR_SEQ 79..114 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_019568" FT MUTAGEN 132 FT /note="R->A: Decreases PS- and PE-dependent ATPase activity FT of ATP11C:TMEM30A; when associated with A-133 and A-136." FT /evidence="ECO:0000269|PubMed:32493773" FT MUTAGEN 133 FT /note="R->A: Decreases PS- and PE-dependent ATPase activity FT of ATP11C:TMEM30A; when associated with A-132 and A-136." FT /evidence="ECO:0000269|PubMed:32493773" FT MUTAGEN 136 FT /note="K->A: Decreases PS- and PE-dependent ATPase activity FT of ATP11C:TMEM30A; when associated with A-132 and A-133." FT /evidence="ECO:0000269|PubMed:32493773" FT TURN 32..36 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 47..73 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 89..91 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 103..112 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 118..126 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 132..135 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 140..143 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 147..151 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 160..163 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 166..170 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 173..176 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:6K7M" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 202..205 FT /evidence="ECO:0007829|PDB:6K7M" FT HELIX 207..211 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 213..215 FT /evidence="ECO:0007829|PDB:7BSV" FT STRAND 218..221 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 223..226 FT /evidence="ECO:0007829|PDB:6K7L" FT TURN 227..229 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:6K7L" FT HELIX 255..261 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 265..276 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 288..296 FT /evidence="ECO:0007829|PDB:6K7L" FT TURN 302..305 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 307..314 FT /evidence="ECO:0007829|PDB:6K7L" FT STRAND 319..321 FT /evidence="ECO:0007829|PDB:6K7N" FT HELIX 324..349 FT /evidence="ECO:0007829|PDB:6K7L" SQ SEQUENCE 361 AA; 40684 MW; 64B3F28C3EB7801B CRC64; MAMNYNAKDE VDGGPPCAPG GTAKTRRPDN TAFKQQRLPA WQPILTAGTV LPIFFIIGLI FIPIGIGIFV TSNNIREIEI DYTGTEPSSP CNKCLSPDVT PCFCTINFTL EKSFEGNVFM YYGLSNFYQN HRRYVKSRDD SQLNGDSSAL LNPSKECEPY RRNEDKPIAP CGAIANSMFN DTLELFLIGN DSYPIPIALK KKGIAWWTDK NVKFRNPPGG DNLEERFKGT TKPVNWLKPV YMLDSDPDNN GFINEDFIVW MRTAALPTFR KLYRLIERKS DLHPTLPAGR YSLNVTYNYP VHYFDGRKRM ILSTISWMGG KNPFLGIAYI AVGSISFLLG VVLLVINHKY RNSSNTADIT I //